NMR-based flux measurements show that both bacterial and human Hsp70 chaperones interact with helical, as well as sheet substrates predominantly through a conformational selection mechanism.

Hsp70 restricts DNA binding activity of Hsf1 to control the width and amplitude of the heat-shock regulon.

Multiple chaperone binding sites on substrates suggest a mechanism by which the Hsp70 chaperone can circumvent kinetic traps in protein folding.

Environmental conditions strongly impact the fitness effects of Hsp90, resulting in the selection of Hsp90 sequences in nature that are robust to a variety of stressful conditions.

Hsp70 chaperone provides Hsp104 with high efficiency in disaggregation and specificity towards aggregated substrates at the, otherwise limiting, cellular concentrations of adenine nucleotides.

A flip of the dimer asymmetry following the first ATP hydrolysis provides a mechanistic model for client remodeling by the mitochondrial Hsp90, TRAP1.

Dynamic regulation of the heat shock response depends on a negative feedback loop in which Hsf1 activates expression of Hsp70 and Hsp70 specifically and directly represses Hsf1 transactivation.

A major cytoplasmic chaperone, Ssa2p, acts as a nuclear import carrier for tRNAs upon nutrient starvation in Saccharomyces cerevisiae.

Cytosolic and organellar Hsp90s from higher eukaryotes have evolved a variable, and environmentally responsive N-terminal extension to regulate their activity.

Food overconsumption impairs cellular protein folding through a novel aging-related signaling pathway.